A common structural theme in histone chaperones mimics interhistone contacts.

Elsässer SJ

Trends Biochem. Sci. 38 (7) 333-336 [2013-07-00; online 2013-06-26]

Histones are among the most conserved proteins in eukaryotes: the structural constraints of the nucleosome pose a challenge to evolving novel function. Nevertheless, confined histone surfaces have diversified, allowing the modulation of basic chromatin function through specialized histone chaperones. Recent structures of three histone-chaperone complexes, DAXX, HJURP, and Scm3, exemplify a common parsimonious solution to the restricted evolutionary space of histone recognition by their cognate histone chaperones: the reutilization of existing themes in histone structural biology.

SciLifeLab Fellow

Simon Elsässer

PubMed 23790282

DOI 10.1016/j.tibs.2013.04.002

Crossref 10.1016/j.tibs.2013.04.002

pii: S0968-0004(13)00061-3

Publications 9.5.0